About: Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations

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About: Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations
Creator	Magistrato, Alessandra Saltalamacchia, Andrea Spinello, Angelo
Source	Medline; PMC; WHO
abstract	[Image: see text] The severe acute respiratory syndrome coronavirus (SARS-CoV-2) pandemic is setting the global health crisis of our time, causing a devastating societal and economic burden. An idiosyncratic trait of coronaviruses is the presence of spike glycoproteins on the viral envelope, which mediate the virus binding to specific host receptor, enabling its entry into the human cells. In spite of the high sequence identity of SARS-CoV-2 with its closely related SARS-CoV emerged in 2002, the atomic-level determinants underlining the molecular recognition of SARS-CoV-2 to the angiotensin-converting enzyme 2 (ACE2) receptor and, thus, the rapid virus spread into human body, remain unresolved. Here, multi-microsecond-long molecular dynamics simulations enabled us to unprecedentedly dissect the key molecular traits liable of the higher affinity/specificity of SARS-CoV-2 toward ACE2 as compared to SARS-CoV. This supplies a minute per-residue contact map underlining its stunningly high infectivity. Harnessing this knowledge is pivotal for urgently developing effective medical countermeasures to face the ongoing global health crisis.
has issue date	2020-05-28(xsd:dateTime)
bibo:doi	10.1021/acs.jpclett.0c01148
bibo:pmid	32463239
has license	no-cc
sha1sum (hex)	4604f147deaf51b908400e233b3f1de62c6cba8d
schema:url	https://doi.org/10.1021/acs.jpclett.0c01148
resource representing a document's title	Is the Rigidity of SARS-CoV-2 Spike Receptor-Binding Motif the Hallmark for Its Enhanced Infectivity? Insights from All-Atom Simulations
has PubMed Central identifier	PMC7274147
has PubMed identifier	32463239
schema:publication	J Phys Chem Lett
resource representing a document's body	covid:4604f147deaf51b908400e233b3f1de62c6cba8d#body_text
is schema:about of	named entity 'economic' named entity 'virus' named entity 'viral envelope' named entity 'SARS-CoV-2' named entity 'Motif' named entity 'ENABLED' named entity 'TRAITS' named entity 'LEVEL' named entity 'VIRUS BINDING' named entity 'LONG' named entity 'MAP' named entity 'devastating' named entity 'receptor' named entity 'pivotal' named entity 'host' named entity 'presence' named entity 'specific' named entity 'effective' named entity '2002' named entity 'trait' named entity 'supplies' named entity 'infectivity' named entity 'ACE2' named entity 'global health' named entity 'coronaviruses' named entity 'health crisis' named entity 'ACE2' named entity 'SARS-CoV-2' named entity 'infectivity' named entity 'microsecond' named entity 'ACE2' named entity 'Receptor' named entity 'SARS-CoV-2' named entity 'Binding Motif' named entity 'This' named entity 'adduct' named entity 'SARS-CoV-2' named entity 'vaccinology' named entity 'ACE2' named entity 'ACE2' named entity 'China' named entity 'SARS-CoV-2' named entity 'Middle East respiratory syndrome coronavirus' named entity 'ACE2' named entity 'World Health Organization' named entity 'β-strands' named entity 'vaccinology' named entity 'receptor recognition' named entity 'adduct' named entity 'molecular dynamics' named entity 'ACE2' named entity 'SARS-CoV' named entity 'ACE2' named entity 'ACE2' named entity 'SARS-CoV' named entity 'acs.org' named entity 'electrostatic repulsion' named entity 'ACE2' named entity 'topological signature' named entity 'SARS-CoV-2' named entity 'angiotensin-converting enzyme 2' named entity 'drug design' named entity 'PDB' named entity 'SARS-CoV' named entity 'RBD' named entity 'adduct' named entity 'ACE2' named entity 'binding affinity' named entity 'mutation' named entity 'SARS-CoV-2' named entity 'peptide' named entity 'Journal of Physical Chemistry Letters' named entity 'structure-based' named entity 'SARS-CoV-2' named entity 'zinc' named entity 'crystal structure' named entity 'surface plasmon resonance' named entity 'ACE2' named entity 'pathogen'

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